ID   A0A0N8QMB1_9PSED        Unreviewed;      1114 AA.
AC   A0A0N8QMB1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-FEB-2019, entry version 12.
DE   RecName: Full=Ribonuclease E {ECO:0000256|HAMAP-Rule:MF_00970};
DE            Short=RNase E {ECO:0000256|HAMAP-Rule:MF_00970};
DE            EC=3.1.26.12 {ECO:0000256|HAMAP-Rule:MF_00970};
GN   Name=rne {ECO:0000256|HAMAP-Rule:MF_00970};
GN   ORFNames=ALO86_03833 {ECO:0000313|EMBL:KPW44294.1}, ALQ06_00675
GN   {ECO:0000313|EMBL:RMQ28120.1};
OS   Pseudomonas syringae pv. berberidis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=251704 {ECO:0000313|EMBL:KPW44294.1, ECO:0000313|Proteomes:UP000050565};
RN   [1] {ECO:0000313|EMBL:KPW44294.1, ECO:0000313|Proteomes:UP000050565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP4116 {ECO:0000313|EMBL:KPW44294.1,
RC   ECO:0000313|Proteomes:UP000050565};
RA   Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT   "Genome announcement of multiple Pseudomonas syringae strains.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RMQ28120.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ICMP 4065 {ECO:0000313|EMBL:RMQ28120.1};
RA   Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.;
RT   "Recombination of ecologically and evolutionarily significant loci
RT   maintains genetic cohesion in the Pseudomonas syringae species
RT   complex.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endoribonuclease that plays a central role in RNA
CC       processing and decay. Required for the maturation of 5S and 16S
CC       rRNAs and the majority of tRNAs. Also involved in the degradation
CC       of most mRNAs. {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and
CC         U-rich regions.; EC=3.1.26.12; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00970};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC       Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00970};
CC   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation. Within
CC       the RNA degradosome, Rnase E assembles into a homotetramer formed
CC       by a dimer of dimers. {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}.
CC       Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral
CC       membrane protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic
CC       side {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPW44294.1}.
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DR   EMBL; LJPU01000327; KPW44294.1; -; Genomic_DNA.
DR   EMBL; RBRC01000355; RMQ28120.1; -; Genomic_DNA.
DR   EnsemblBacteria; KPW44294; KPW44294; ALO86_03833.
DR   PATRIC; fig|251704.3.peg.5071; -.
DR   Proteomes; UP000050565; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00970; RNase_E; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR028878; RNase_E.
DR   InterPro; IPR004659; RNase_E/G.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00757; RNaseEG; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050565};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   DOMAIN       39    117       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      401    404       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   COILED      314    334       {ECO:0000256|SAM:Coils}.
FT   COILED     1056   1076       {ECO:0000256|SAM:Coils}.
FT   METAL       300    300       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       343    343       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       401    401       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   METAL       404    404       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
SQ   SEQUENCE   1114 AA;  122335 MW;  26A29969AFF42869 CRC64;
     MKRMLINATQ PEELRVALVD GQRLYDLDIE SGAREQKKAN IYKGRITRIE PSLEAAFVDF
     GSERHGFLPL KEISREYFKK APEGRVNIKD VLSEGQEVIV QVEKEERGNK GAALTTFISL
     AGRYLVLMPN NPRAGGISRR IEGEERNELR EALNGLIAPA DMGLIVRTAG LGRSSEEMQW
     DLDYLLQLWT AIKEASLDRS APFLIYQESN VIIRAIRDYL RQDIGEVLID SVEAQEEALT
     FIRQVMPQYA SKIKLYEDSV PLFNRFQIES QIETAFQRVV ELPSGGSIVI DPTEALVSID
     INSARATKGS DIEETALQTN LEAAEEIARQ LRLRDIGGLI VIDFIDMTPA KNQRAVEEKV
     RESLEADRAR VQVGRISRFG LLEMSRQRLR PSLGESSGIV CPRCNGTGII RDVESLSLAI
     LRLIEEEALK DRTAEVRAQV PIPVAAFLLN EKRNSITKIE LRTRARIIIL PNDQLETPHF
     EVQRLRDDSP EAHNSQTSYE IAAAAAAAEV EEIAPLAAAT RTLVRQEAAV KTAPARANAP
     VPVEVAAPAP TPAPVAHEPS LFKGLVKSLV SLFATKEEPV VAPAVVEKPA AEQRPARNEE
     RRNGRQQSRG RNNRRDEERK PREERAPREE RAERAPREER APREERAPRE ERAVREPREA
     REESAPREER PARTSRERKP REAREDRPVR ELREPLDAVA TAAQAGPAVN LAREERPERA
     PREERQPRAP REERQPRAEQ AAVAVSEEEE VLLNDEQAND DNQDGNDGSE GDRPRRRSRG
     QRRRSNRRER QRDANGNVIE GSEENGSEEN GAEETVNDED NSATDLSAGL GFTAAAASGV
     ISATAEADAH QQAERANSTT QSAPAAEPVQ QAAVAHAPVV ETPAVEAPVA ETSAVETPAP
     QAPAAEQTAE VPAVEAPVAD DAPVAQPAPE VEVQPAAVEA PAIAAQTELF EAPHAERVVP
     FTPTPAPAPQ APVEAAAHEQ VPATESSELP TPVEAPAAEP AAFVKDEPAP YIAPQAAVEE
     QASAPAEQEP VIVETPAVPV SSTGRAPNDP REVRRRKREE EARRQQETTA ASAQAESAQP
     SQATEEKTDV ATTEQPAVQP HHDAEKETEP KPLV
//